Determination of Translational Velocity of Reaction Mixture Components: Effect on the Rate of Reaction

Ikechukwu Iloh Udema

doi:doi:10.11648/j.ab.20160406.13

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Determination of Translational Velocity of Reaction Mixture Components: Effect on the Rate of Reaction

Ikechukwu Iloh Udema

Published in Advances in Biochemistry (Volume 4, Issue 6)

Received: 31 October 2016 Accepted: 16 November 2016 Published: 16 December 2016

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Abstract

The objectives of the research were to: 1) formulate a simple mathematical model for the determination of initial velocity and terminal velocity of dissolved solute in aqueous solvent, 2) to determine the minimum interparticle distance (l_EM) for which the periods of coverage determined according two methods namely Einstein model and Newtonian model are equal and 3) elucidate the importance of translational velocity and the minimum interparticle distance in the optimization of the purpose of enzyme catalyzed reaction. The values of l_EM for which Einstein and Newtonian approach for the determination of time for the coverage of such distance gave the same result were 3.15 exp (-8) m and 4.04 exp (-8) m when the concentrations of enzyme were ~ 2.4 exp (-8) mol/l and ~3.21 exp (-8) mo/l respectively. The terminal velocity was ~ 8.43 nm/s at 293.15K; the real/effective kinetic energy in solution was ~7.36 exp (-27) J at 293.15K. The initial velocity of solute was ~ 9.25 exp (-3) m/s. In conclusion, a model for the determination of terminal velocity and initial velocity was derived. The initial velocity is » the terminal velocity at a given temperature. Effective collision between the bullet molecule and the much larger target molecule at l_EM or less should be directional so as to achieve enzyme-substrate and drug-pathogen/poison complex formation.

Published in	Advances in Biochemistry (Volume 4, Issue 6)
DOI	10.11648/j.ab.20160406.13
Page(s)	84-93
Creative Commons	This is an Open Access article, distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution and reproduction in any medium or format, provided the original work is properly cited.
Copyright	Copyright © The Author(s), 2024. Published by Science Publishing Group

Keywords

Aspergillus Oryzea Alpha Amylase, Model, Translational Velocity, Ballistic and Brownian Time, Minimum Interparticle Distance

References

[1]	Roosen-Runge, F.; Hennig, M.; Zhang, F.; Jacobs, RMJ.; Sztucki, M.; Schober, H.; Seydel, T.; and Schreiber, F.; 2011. Protein self-diffusion in crowded solutions. Proceedings of National Academy of Science USA108 (29):11815–11820.
[2]	Martin, V.; Aubertin, M.; Bussière, B.; Mbonimpa, M.; Dagenais, A-M.; and Gosselin, M.; 2006 Measurement of oxygen consumption and diffusion in exposed and covered reactive mine tailings. 7th International conference on acid rock drainage (ICARD). American Society of Mining and Reclamation (ASMR), 3134 Montavesta Road, Lexington, KY 40502.
[3]	Wade, RC.; Gabdoulline, RR.; LU ¨Demann, SK.; and`Re Lounnas, V. 1998. Electrostatic steering and ionic tethering in enzyme–ligand binding: Insights from simulations. Proceedings of National Academy of Science USA. 95: 5942–5949.
[4]	Wade, RC.; Gabdoulline, RR.; LU ¨Demann, SK.; and`Re Lounnas, V. 1998. Electrostatic steering and ionic tethering in enzyme–ligand binding: Insights from simulations. Proceedings of National Academy of Science USA. 95: 5942–5949.
[5]	Bernzzani, P.; 2008. Structural changes associated with interactions between starch and particles of TiO2 or ZnSe Journal of Biological Chemistry and Molecular Biology. 2(1), 1-13.
[6]	Van Oijen, AM.; 2008. Cutting the forest to see a single? Nature Chemical Biology. 4 (8): 440-443.
[7]	Ahmedi, A.; Abouseoud, M.; Abdeltif, A.; and Annabelle, C.; 2015. Effect of diffusion on discoloration of Congo red by alginate entrapped turnip (Brassica rapa) peroxidase Enzyme Research. 2015: 1-9.
[8]	Northrop, JH.; and Anson, ML.; 1928. A method for the determination of diffusion constants and the calculation of the radius and weight of the haemoglobin molecules Journal of General Physiology. 12 (2): 549-552.
[9]	Quillin, ML.; and Matthews, BW.; 2000. Accurate calculation of the density of proteins. Acta Crystallographica D56: 791-794.
[10]	Fisher, H.; Polikarpov, I.; and Craievich, AF.; 2004. Average protein density is a molecular-weight-dependent function. Protein Science. 13:2825-2828.
[11]	D’ Amico, S.; Marx, J–C.; Gerday, C.; and Feller, G.; 2003. Activity–stability relationships in extremophilic enzymes Journal of Biological Chemistry. 276(10): 7891–7896.
[12]	Moyer, LS.; and Abramson, HA.; 1938. Electrokinetic aspects of surface chemistry v. Electric mobility and titration curves of proteins and their relationship to the calculation of radius and molecular weight. Journal of Biological Chemistry. 123: 391-403.
[13]	Morar, AS.; Olteanu, A.; Young, GB.; and Pielak, GJ.;2001. Solvent-induced collapse of alpha synuclein and acid-denatured cytochrome C. Protein Science. 10: 2195-2199.
[14]	Sugahara, M.; Takehira, M.; and Yutani, K.; 2013. Effect of heavy atoms on the thermal stability of alpha amylase from Aspergillus oryzea. PlosOne. 8(2):1–7.
[15]	Sky-Peck, HH.; and Thuvasethakul, P.; 1977. Human Pancreatic alpha amylase I. Purification and characterization Annals of Clinical Laboratory Science. 7(4): 298-309.
[16]	Bernfeld, P.; 1955. Amylases, alpha and beta. Methods in Enzymology. 1:149-152.
[17]	D’ Amico, S.; Gerday, C.; Feller, G.; 2002. Structural determinants of cold adaptation and stability in a psychrophilic alpha–amylase. Biologia, Bratislava, 57/Supplement. 11:213-219.
[18]	Low, PS.; Bada, JL.; and Somero, GN.; 1973. Temperature adaptation of enzymes: Roles of the free energy, the enthalpy, and entropy of activation Proceedings of National Academy of Science U.S.A. 70(2): 430–432.
[19]	Stylianopoulos, T.; Poh, M-Z.; Insin, N.; Bawendi, MG.; Fukumura, D.; Munn, LL.; and Jain, RK.; 2010. Diffusion of particles in the extracellular matrix: The effect of repulsive electrostatic interactions. Biophysical Journal. 99: 1342-1349.
[20]	Szabo, A.; and Zhoub, H-X.; 2012. Role of diffusion in the kinetics of reversible enzyme-catalyzed reactions. Bulletin of Korean Chemical Society. 33(3): 925-928.
[21]	Kim, JS.; and Yethiraj, A.; Effect of macromolecular crowding on reaction rates: A computational and theoretical study Biophysical Journal. 2009;96: 1333-1340.
[22]	Berezhkovskii, AM.; Szabo, A.; Zhou, and H-Z.; 2011. Diffusion-influenced ligand binding to buried sites in macromolecules and transmembrane channels. Journal of Chemical Physics. 135:1-5.
[23]	Blom, J.; and Schwarz, B.; Potato starch as substrate for determination of diastatic activity First International Congress of Biochemistry (Section XII), Cambridge 1945; 1-5.
[24]	Xie, Y.; Yan, M.; Yuan, S.; Sun, S.; and Huo, Q.; 2013. Effect of microwave treatment on the physiological properties of potato starch granules. Chemistry Central Journal. 7: 1-7.
[25]	Butterworth, JP.; Warren, FW.; and Ellis, PR.; 2011. Human alpha amylase and starch digestion: An interesting marriage. Starch/Stärke, 63: 395-405.
[26]	Huggins, C.; and Russell, PS.; 1948. Colorimetric determination of amylase. Annals of Surgery, 128 (4): 668-678.
[27]	Schnell, S.; and Maini, PK.; 2000. Enzyme Kinetics at High Enzyme Concentration. Bulletin Mathematical Biology, 62: 483-499.

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APA Style

Ikechukwu Iloh Udema. (2016). Determination of Translational Velocity of Reaction Mixture Components: Effect on the Rate of Reaction. Advances in Biochemistry, 4(6), 84-93. https://doi.org/10.11648/j.ab.20160406.13

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ACS Style

Ikechukwu Iloh Udema. Determination of Translational Velocity of Reaction Mixture Components: Effect on the Rate of Reaction. Adv. Biochem. 2016, 4(6), 84-93. doi: 10.11648/j.ab.20160406.13

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AMA Style

Ikechukwu Iloh Udema. Determination of Translational Velocity of Reaction Mixture Components: Effect on the Rate of Reaction. Adv Biochem. 2016;4(6):84-93. doi: 10.11648/j.ab.20160406.13

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@article{10.11648/j.ab.20160406.13,
  author = {Ikechukwu Iloh Udema},
  title = {Determination of Translational Velocity of Reaction Mixture Components: Effect on the Rate of Reaction},
  journal = {Advances in Biochemistry},
  volume = {4},
  number = {6},
  pages = {84-93},
  doi = {10.11648/j.ab.20160406.13},
  url = {https://doi.org/10.11648/j.ab.20160406.13},
  eprint = {https://article.sciencepublishinggroup.com/pdf/10.11648.j.ab.20160406.13},
  abstract = {The objectives of the research were to: 1) formulate a simple mathematical model for the determination of initial velocity and terminal velocity of dissolved solute in aqueous solvent, 2) to determine the minimum interparticle distance (lEM) for which the periods of coverage determined according two methods namely Einstein model and Newtonian model are equal and 3) elucidate the importance of translational velocity and the minimum interparticle distance in the optimization of the purpose of enzyme catalyzed reaction. The values of lEM for which Einstein and Newtonian approach for the determination of time for the coverage of such distance gave the same result were 3.15 exp (-8) m and 4.04 exp (-8) m when the concentrations of enzyme were ~ 2.4 exp (-8) mol/l and ~3.21 exp (-8) mo/l respectively. The terminal velocity was ~ 8.43 nm/s at 293.15K; the real/effective kinetic energy in solution was ~7.36 exp (-27) J at 293.15K. The initial velocity of solute was ~ 9.25 exp (-3) m/s. In conclusion, a model for the determination of terminal velocity and initial velocity was derived. The initial velocity is » the terminal velocity at a given temperature. Effective collision between the bullet molecule and the much larger target molecule at lEM or less should be directional so as to achieve enzyme-substrate and drug-pathogen/poison complex formation.},
 year = {2016}
}

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TY  - JOUR
T1  - Determination of Translational Velocity of Reaction Mixture Components: Effect on the Rate of Reaction
AU  - Ikechukwu Iloh Udema
Y1  - 2016/12/16
PY  - 2016
N1  - https://doi.org/10.11648/j.ab.20160406.13
DO  - 10.11648/j.ab.20160406.13
T2  - Advances in Biochemistry
JF  - Advances in Biochemistry
JO  - Advances in Biochemistry
SP  - 84
EP  - 93
PB  - Science Publishing Group
SN  - 2329-0862
UR  - https://doi.org/10.11648/j.ab.20160406.13
AB  - The objectives of the research were to: 1) formulate a simple mathematical model for the determination of initial velocity and terminal velocity of dissolved solute in aqueous solvent, 2) to determine the minimum interparticle distance (lEM) for which the periods of coverage determined according two methods namely Einstein model and Newtonian model are equal and 3) elucidate the importance of translational velocity and the minimum interparticle distance in the optimization of the purpose of enzyme catalyzed reaction. The values of lEM for which Einstein and Newtonian approach for the determination of time for the coverage of such distance gave the same result were 3.15 exp (-8) m and 4.04 exp (-8) m when the concentrations of enzyme were ~ 2.4 exp (-8) mol/l and ~3.21 exp (-8) mo/l respectively. The terminal velocity was ~ 8.43 nm/s at 293.15K; the real/effective kinetic energy in solution was ~7.36 exp (-27) J at 293.15K. The initial velocity of solute was ~ 9.25 exp (-3) m/s. In conclusion, a model for the determination of terminal velocity and initial velocity was derived. The initial velocity is » the terminal velocity at a given temperature. Effective collision between the bullet molecule and the much larger target molecule at lEM or less should be directional so as to achieve enzyme-substrate and drug-pathogen/poison complex formation.
VL  - 4
IS  - 6
ER  -

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Author Information

Ikechukwu Iloh Udema

Ude International Concepts Ltd., B. B. Agbor, Nigeria

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Plain Text BibTeX RIS

APA Style

Ikechukwu Iloh Udema. (2016). Determination of Translational Velocity of Reaction Mixture Components: Effect on the Rate of Reaction. Advances in Biochemistry, 4(6), 84-93. https://doi.org/10.11648/j.ab.20160406.13

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ACS Style

Ikechukwu Iloh Udema. Determination of Translational Velocity of Reaction Mixture Components: Effect on the Rate of Reaction. Adv. Biochem. 2016, 4(6), 84-93. doi: 10.11648/j.ab.20160406.13

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AMA Style

Ikechukwu Iloh Udema. Determination of Translational Velocity of Reaction Mixture Components: Effect on the Rate of Reaction. Adv Biochem. 2016;4(6):84-93. doi: 10.11648/j.ab.20160406.13

Copy | Download

@article{10.11648/j.ab.20160406.13,
  author = {Ikechukwu Iloh Udema},
  title = {Determination of Translational Velocity of Reaction Mixture Components: Effect on the Rate of Reaction},
  journal = {Advances in Biochemistry},
  volume = {4},
  number = {6},
  pages = {84-93},
  doi = {10.11648/j.ab.20160406.13},
  url = {https://doi.org/10.11648/j.ab.20160406.13},
  eprint = {https://article.sciencepublishinggroup.com/pdf/10.11648.j.ab.20160406.13},
  abstract = {The objectives of the research were to: 1) formulate a simple mathematical model for the determination of initial velocity and terminal velocity of dissolved solute in aqueous solvent, 2) to determine the minimum interparticle distance (lEM) for which the periods of coverage determined according two methods namely Einstein model and Newtonian model are equal and 3) elucidate the importance of translational velocity and the minimum interparticle distance in the optimization of the purpose of enzyme catalyzed reaction. The values of lEM for which Einstein and Newtonian approach for the determination of time for the coverage of such distance gave the same result were 3.15 exp (-8) m and 4.04 exp (-8) m when the concentrations of enzyme were ~ 2.4 exp (-8) mol/l and ~3.21 exp (-8) mo/l respectively. The terminal velocity was ~ 8.43 nm/s at 293.15K; the real/effective kinetic energy in solution was ~7.36 exp (-27) J at 293.15K. The initial velocity of solute was ~ 9.25 exp (-3) m/s. In conclusion, a model for the determination of terminal velocity and initial velocity was derived. The initial velocity is » the terminal velocity at a given temperature. Effective collision between the bullet molecule and the much larger target molecule at lEM or less should be directional so as to achieve enzyme-substrate and drug-pathogen/poison complex formation.},
 year = {2016}
}

Copy | Download

TY  - JOUR
T1  - Determination of Translational Velocity of Reaction Mixture Components: Effect on the Rate of Reaction
AU  - Ikechukwu Iloh Udema
Y1  - 2016/12/16
PY  - 2016
N1  - https://doi.org/10.11648/j.ab.20160406.13
DO  - 10.11648/j.ab.20160406.13
T2  - Advances in Biochemistry
JF  - Advances in Biochemistry
JO  - Advances in Biochemistry
SP  - 84
EP  - 93
PB  - Science Publishing Group
SN  - 2329-0862
UR  - https://doi.org/10.11648/j.ab.20160406.13
AB  - The objectives of the research were to: 1) formulate a simple mathematical model for the determination of initial velocity and terminal velocity of dissolved solute in aqueous solvent, 2) to determine the minimum interparticle distance (lEM) for which the periods of coverage determined according two methods namely Einstein model and Newtonian model are equal and 3) elucidate the importance of translational velocity and the minimum interparticle distance in the optimization of the purpose of enzyme catalyzed reaction. The values of lEM for which Einstein and Newtonian approach for the determination of time for the coverage of such distance gave the same result were 3.15 exp (-8) m and 4.04 exp (-8) m when the concentrations of enzyme were ~ 2.4 exp (-8) mol/l and ~3.21 exp (-8) mo/l respectively. The terminal velocity was ~ 8.43 nm/s at 293.15K; the real/effective kinetic energy in solution was ~7.36 exp (-27) J at 293.15K. The initial velocity of solute was ~ 9.25 exp (-3) m/s. In conclusion, a model for the determination of terminal velocity and initial velocity was derived. The initial velocity is » the terminal velocity at a given temperature. Effective collision between the bullet molecule and the much larger target molecule at lEM or less should be directional so as to achieve enzyme-substrate and drug-pathogen/poison complex formation.
VL  - 4
IS  - 6
ER  -

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